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O43164

- PJA2_HUMAN

UniProt

O43164 - PJA2_HUMAN

Protein

E3 ubiquitin-protein ligase Praja-2

Gene

PJA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 4 (24 Nov 2009)
      Previous versions | rss
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    Functioni

    Has E2-dependent E3 ubiquitin-protein ligase activity. Responsible for ubiquitination of cAMP-dependent protein kinase type I and type II-alpha/beta regulatory subunits and for targeting them for proteasomal degradation. Essential for PKA-mediated long-term memory processes.2 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri634 – 67542RING-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein kinase A catalytic subunit binding Source: UniProtKB
    3. protein kinase A regulatory subunit binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. long-term memory Source: UniProtKB
    2. protein ubiquitination Source: UniProtKB
    3. regulation of protein kinase A signaling Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase Praja-2 (EC:6.3.2.-)
    Short name:
    Praja2
    Alternative name(s):
    RING finger protein 131
    Gene namesi
    Name:PJA2
    Synonyms:KIAA0438, RNF131
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:17481. PJA2.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication. Endoplasmic reticulum membrane 1 Publication; Peripheral membrane protein 1 Publication. Golgi apparatus membrane 1 Publication; Peripheral membrane protein 1 Publication. Cell junctionsynapse By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity
    Note: Localizes at the cytoplasmic side of endoplasmic reticulum and Golgi apparatus. Expressed in the postsynaptic density region of synapses By similarity. Colocalizes with PRKAR2A and PRKAR2B in the cytoplasm and the cell membrane.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. Golgi membrane Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB
    6. postsynaptic density Source: UniProtKB-SubCell
    7. postsynaptic membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134873520.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 708707E3 ubiquitin-protein ligase Praja-2PRO_0000278230Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei309 – 3091Phosphoserine1 Publication
    Modified residuei323 – 3231Phosphoserine1 Publication
    Modified residuei342 – 3421Phosphoserine; by PKA1 Publication
    Modified residuei389 – 3891Phosphothreonine; by PKA1 Publication
    Modified residuei432 – 4321Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO43164.
    PaxDbiO43164.
    PRIDEiO43164.

    PTM databases

    PhosphoSiteiO43164.

    Expressioni

    Gene expression databases

    BgeeiO43164.
    CleanExiHS_PJA2.
    GenevestigatoriO43164.

    Organism-specific databases

    HPAiHPA040347.

    Interactioni

    Subunit structurei

    Binds ubiquitin-conjugating enzymes (E2s). In vitro, interacts with the ubiquitin-conjugating enzyme, UBE2D2. The phosphorylated form interacts with PRKAR1A, PRKAR2A and PRKAR2B. Binds the catalytic subunits of cAMP-dependent protein kinase.2 Publications

    Protein-protein interaction databases

    BioGridi115200. 20 interactions.
    DIPiDIP-47040N.
    IntActiO43164. 16 interactions.
    STRINGi9606.ENSP00000354775.

    Structurei

    3D structure databases

    ProteinModelPortaliO43164.
    SMRiO43164. Positions 603-680.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni531 – 708178Interaction with PRKAR1A, PRKAR2A and PRKAR2BAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri634 – 67542RING-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG272750.
    HOGENOMiHOG000230900.
    HOVERGENiHBG003815.
    InParanoidiO43164.
    KOiK10634.
    OMAiEFAQPEA.
    OrthoDBiEOG7TJ3HJ.
    PhylomeDBiO43164.
    TreeFamiTF330711.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF13639. zf-RING_2. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43164-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSQYTEKEPA AMDQESGKAV WPKPAGGYQT ITGRRYGRRH AYVSFKPCMT    50
    RHERSLGRAG DDYEVLELDD VPKENSSGSS PLDQVDSSLP SEPIFEKSET 100
    EIPTCGSALN QTTESSQSFV AVHHSEEGRD TLGSSTNLHN HSEGEYIPGA 150
    CSASSVQNGI ALVHTDSYDP DGKHGEDNDH LQLSAEVVEG SRYQESLGNT 200
    VFELENREAE AYTGLSPPVP SFNCEVRDEF EELDSVPLVK SSAGDTEFVH 250
    QNSQEIQRSS QDEMVSTKQQ NNTSQERQTE HSPEDAACGP GHICSEQNTN 300
    DREKNHGSSP EQVVRPKVRK LISSSQVDQE TGFNRHEAKQ RSVQRWREAL 350
    EVEESGSDDL LIKCEEYDGE HDCMFLDPPY SRVITQRETE NNQMTSESGA 400
    TAGRQEVDNT FWNGCGDYYQ LYDKDEDSSE CSDGEWSASL PHRFSGTEKD 450
    QSSSDESWET LPGKDENEPE LQSDSSGPEE ENQELSLQEG EQTSLEEGEI 500
    PWLQYNEVNE SSSDEGNEPA NEFAQPAFML DGNNNLEDDS SVSEDLDVDW 550
    SLFDGFADGL GVAEAISYVD PQFLTYMALE ERLAQAMETA LAHLESLAVD 600
    VEVANPPASK ESIDGLPETL VLEDHTAIGQ EQCCPICCSE YIKDDIATEL 650
    PCHHFFHKPC VSIWLQKSGT CPVCRRHFPP AVIEASAAPS SEPDPDAPPS 700
    NDSIAEAP 708
    Length:708
    Mass (Da):78,214
    Last modified:November 24, 2009 - v4
    Checksum:i719B4A367C411735
    GO
    Isoform 2 (identifier: O43164-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         544-563: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:688
    Mass (Da):76,091
    Checksum:i34A652ACAF3A02FE
    GO

    Sequence cautioni

    The sequence BAA23710.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti176 – 1761E → G.
    Corresponds to variant rs35224970 [ dbSNP | Ensembl ].
    VAR_057215
    Natural varianti297 – 2971Q → R.2 Publications
    Corresponds to variant rs1045706 [ dbSNP | Ensembl ].
    VAR_030698
    Natural varianti705 – 7051A → T.
    Corresponds to variant rs246105 [ dbSNP | Ensembl ].
    VAR_030699

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei544 – 56320Missing in isoform 2. 1 PublicationVSP_023198Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007898 mRNA. Translation: BAA23710.2. Different initiation.
    AK291759 mRNA. Translation: BAF84448.1.
    AC008467 Genomic DNA. No translation available.
    AC010625 Genomic DNA. No translation available.
    CH471086 Genomic DNA. Translation: EAW49050.1.
    CH471086 Genomic DNA. Translation: EAW49051.1.
    BC030826 mRNA. Translation: AAH30826.1.
    CR749579 mRNA. Translation: CAH18371.1.
    CCDSiCCDS4099.1. [O43164-1]
    PIRiT00064.
    RefSeqiNP_055634.3. NM_014819.4. [O43164-1]
    UniGeneiHs.483036.

    Genome annotation databases

    EnsembliENST00000361189; ENSP00000354775; ENSG00000198961. [O43164-1]
    ENST00000361557; ENSP00000355284; ENSG00000198961. [O43164-1]
    GeneIDi9867.
    KEGGihsa:9867.
    UCSCiuc003kos.4. human. [O43164-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007898 mRNA. Translation: BAA23710.2 . Different initiation.
    AK291759 mRNA. Translation: BAF84448.1 .
    AC008467 Genomic DNA. No translation available.
    AC010625 Genomic DNA. No translation available.
    CH471086 Genomic DNA. Translation: EAW49050.1 .
    CH471086 Genomic DNA. Translation: EAW49051.1 .
    BC030826 mRNA. Translation: AAH30826.1 .
    CR749579 mRNA. Translation: CAH18371.1 .
    CCDSi CCDS4099.1. [O43164-1 ]
    PIRi T00064.
    RefSeqi NP_055634.3. NM_014819.4. [O43164-1 ]
    UniGenei Hs.483036.

    3D structure databases

    ProteinModelPortali O43164.
    SMRi O43164. Positions 603-680.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115200. 20 interactions.
    DIPi DIP-47040N.
    IntActi O43164. 16 interactions.
    STRINGi 9606.ENSP00000354775.

    PTM databases

    PhosphoSitei O43164.

    Proteomic databases

    MaxQBi O43164.
    PaxDbi O43164.
    PRIDEi O43164.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361189 ; ENSP00000354775 ; ENSG00000198961 . [O43164-1 ]
    ENST00000361557 ; ENSP00000355284 ; ENSG00000198961 . [O43164-1 ]
    GeneIDi 9867.
    KEGGi hsa:9867.
    UCSCi uc003kos.4. human. [O43164-1 ]

    Organism-specific databases

    CTDi 9867.
    GeneCardsi GC05M108698.
    H-InvDB HIX0005075.
    HGNCi HGNC:17481. PJA2.
    HPAi HPA040347.
    neXtProti NX_O43164.
    PharmGKBi PA134873520.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG272750.
    HOGENOMi HOG000230900.
    HOVERGENi HBG003815.
    InParanoidi O43164.
    KOi K10634.
    OMAi EFAQPEA.
    OrthoDBi EOG7TJ3HJ.
    PhylomeDBi O43164.
    TreeFami TF330711.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi PJA2. human.
    GeneWikii PJA2.
    GenomeRNAii 9867.
    NextBioi 37195.
    PROi O43164.

    Gene expression databases

    Bgeei O43164.
    CleanExi HS_PJA2.
    Genevestigatori O43164.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF13639. zf-RING_2. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
      Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-297.
      Tissue: Brain.
    2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Placenta.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-297.
      Tissue: Brain.
    7. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-18; 24-34; 59-73; 193-207; 241-258; 388-404 AND 583-610, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 456-708 (ISOFORM 2).
      Tissue: Liver.
    9. "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain."
      Yu P., Chen Y., Tagle D.A., Cai T.
      Genomics 79:869-874(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UBE2D2.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRKAR1A; PRKAR2A AND PRKAR2B, PHOSPHORYLATION AT SER-342 AND THR-389.
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPJA2_HUMAN
    AccessioniPrimary (citable) accession number: O43164
    Secondary accession number(s): A8K6U4
    , D3DSZ5, Q68D49, Q8N1G5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 20, 2007
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 119 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3